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The Open Protein Structure Annotation Network
PDB Keyword
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2hqy

    Table of contents
    1. 1. Protein Summary
    2. 2. Ligand Summary

    Title Crystal structure of conserved hypothetical protein from Bacteroides thetaiotaomicron VPI-5482. To be Published
    Site MCSG
    PDB Id 2hqy Target Id
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    Molecular Characteristics
    Source
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    Alias Ids
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    TPS5676,AAO78794.1, 226186
    Molecular Weight
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    Da.
    Residues
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    Isoelectric Point
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    Sequence
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      BLAST   FFAS

    Structure Determination
    Method XRAY
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    Chains 2
    Resolution (Å)
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    Rfree
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    Matthews' coefficent 2.65 Rfactor 0.17559
    Waters
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    Solvent Content 53.65

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    Ligand Information
    Ligands COA (COENZYME) x 1
    Metals

    Jmol

     
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    Google Scholar output for 2hqy
    1. Assessment of predictions submitted for the CASP7 function prediction category
    G Lopez, A Rojas, M Tress - : Structure, Function, and , 2007 - Wiley Online Library
     
    2. Prediction of protein structure from ideal forms
    WR Taylor, GJ Bartlett, V Chelliah - Proteins: Structure, , 2008 - Wiley Online Library
     
    3. Domain definition and target classification for CASP7
    ND Clarke, I Ezkurdia, J Kopp, RJ Read - Proteins: Structure, , 2007 - Wiley Online Library
     
    4. Ligands in PSI structures
    A Kumar, HJ Chiu, HL Axelrod, A Morse - Section F: Structural , 2010 - scripts.iucr.org
     
    5. Reconstruction of Protein Backbone with the alpha-Carbon Coordinates
    JH Wang, CB Yang, CT Tseng - Journal of Information Science , 2010 - etd.lib.nsysu.edu.tw
     
    6. Reconstruction of Protein Backbone with the a-Carbon Coordinates
    JH Wang, CB Yang, CT Tseng - 2007 - asiair.asia.edu.tw
     
    7. Refinement of All-atom Backbone Prediction of Proteins
    HY Chang - 2008 - etd.lib.nsysu.edu.tw
     

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    Protein Summary

    This Bacteroides thetaiotaomicron protein contains two repeats of the Acyl-CoA N-acyltransferase (Nat) fold, a 3 layer alpha/beta/alpha fold with a mixed central beta sheet. Overall topology, with the NAT domain duplication accompanied with the internal swap of C-terminal strand of one of the domains, is similar to that of FemX peptidyltransferase (1ne9), which is involved in the synthesis of the bacterial cell wall, by catalyzing the addition of amino acid(s) on the peptidoglycan precursor using aminoacylated tRNA as a substrate. Significant structural similarity (3A RMSD over 265 aminoacids) between the B. thetaiotaomicron protein and FemX protein 1ne9, suggests possible functional similarity of these two families, despite very low sequence similarity (~6% seq id).

    Ligand Summary

    Reviews

    References

     

    No references found.

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